Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden; Science for Life Laboratory, Stockholm University, Box 1031, SE-171 21 Solna, Sweden.
FEBS Lett. 2014 May 21;588(10):1930-4. doi: 10.1016/j.febslet.2014.03.050. Epub 2014 Apr 12.
Transmembrane helices (TMHs) in membrane proteins can be orientated with their N-terminus towards the cytoplasm (Nin), or facing the non-cytoplasmic side (Nout). Most membrane proteins are inserted co-translationally into membranes, aided by Sec-type translocons. Since the final orientation of Nin- and Nout-orientated TMHs differs, they could also interact differently with the translocon and the surrounding membrane during insertion. We measured pulling forces exerted on Nin-orientated TMHs during co-translational insertion into the inner membrane of Escherichia coli. Our results demonstrate that Nin-orientated TMHs experience a weaker pulling force but retain the overall biphasic force profile seen previously for Nout-orientated TMHs (Ismail et al., 2012 [1]).
膜蛋白中的跨膜螺旋(TMHs)可以将其 N 端朝向细胞质(Nin),或者朝向非细胞质侧(Nout)。大多数膜蛋白都是在 Sec 型转位酶的辅助下共翻译插入膜中的。由于 Nin 和 Nout 定向的 TMHs 的最终取向不同,它们在插入过程中也可能与转位酶和周围膜的相互作用方式不同。我们测量了在大肠杆菌内膜中共翻译插入过程中对 Nin 定向 TMHs 施加的拉力。我们的结果表明,Nin 定向 TMHs 经历的拉力较弱,但保留了以前观察到的 Nout 定向 TMHs 的整体双相力谱(Ismail 等人,2012[1])。